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Volumn 1814, Issue 5, 2011, Pages 713-723

Effect of protein-surfactant interactions on aggregation of β-lactoglobulin

Author keywords

Emulsifier; Isothermal titration calorimetry; Sodium dodecyl sulfate; Surfactant; Thermal stabilization; Whey protein aggregate

Indexed keywords

AMMONIUM CHLORIDE; BETA LACTOGLOBULIN; DODECYL SULFATE SODIUM; MONOMER; PYRANOSIDE; SODIUM SULFATE; SURFACTANT;

EID: 79955612856     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2011.03.011     Document Type: Article
Times cited : (75)

References (54)
  • 1
    • 0032053268 scopus 로고    scopus 로고
    • Molecular basis of protein functionality with special consideration of cold-set gels derived from hat-denatured whey
    • DOI 10.1016/S0924-2244(98)00031-4, PII S0924224498000314
    • C.M. Bryant, and D.J. McClements Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey Trends Food Sci. Tech. 9 1998 143 151 (Pubitemid 28348656)
    • (1998) Trends in Food Science and Technology , vol.9 , Issue.4 , pp. 143-151
    • Bryant, C.M.1    Julian McClements, D.2
  • 2
    • 44549084148 scopus 로고    scopus 로고
    • Whey and whey proteins-from 'gutter-to-gold'
    • G.W. Smithers Whey and whey proteins-from 'gutter-to-gold' Int. Dairy J. 18 (7) 2008 695 704
    • (2008) Int. Dairy J. , vol.187 , pp. 695-704
    • Smithers, G.W.1
  • 3
    • 0032016551 scopus 로고    scopus 로고
    • Nutritional and functional characteristics of whey proteins in food products
    • J.N. De Wit Nutritional and functional characteristics of whey proteins in food products J. Dairy Sci. 81 1998 597
    • (1998) J. Dairy Sci. , vol.81 , pp. 597
    • De Wit, J.N.1
  • 4
    • 0034684168 scopus 로고    scopus 로고
    • The lipocalin protein family: Structural and sequence overview
    • D.R. Flower, A.C.T. North, and C.E. Sansom The lipocalin protein family: structural and sequence overview BBA-Protein Struct. M. 1482 2000 9 24
    • (2000) BBA-Protein Struct. M. , vol.1482 , pp. 9-24
    • Flower, D.R.1    North, A.C.T.2    Sansom, C.E.3
  • 5
    • 33947316219 scopus 로고    scopus 로고
    • Promiscuous Binding of Ligands by β-Lactoglobulin Involves Hydrophobic Interactions and Plasticity
    • DOI 10.1016/j.jmb.2007.01.077, PII S0022283607001544
    • T. Konuma, K. Sakurai, and Y. Goto Promiscuous binding of ligands by beta-lactoglobulin involves hydrophobic interactions and plasticity J. Mol. Biol. 368 2007 209 218 (Pubitemid 46441219)
    • (2007) Journal of Molecular Biology , vol.368 , Issue.1 , pp. 209-218
    • Konuma, T.1    Sakurai, K.2    Goto, Y.3
  • 6
    • 58149196312 scopus 로고    scopus 로고
    • Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 °c. A review
    • J.N. de Wit Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150 °C. A review Trends Food Sci. Tech. 20 2009 27 34
    • (2009) Trends Food Sci. Tech. , vol.20 , pp. 27-34
    • De Wit, J.N.1
  • 7
    • 0036704306 scopus 로고    scopus 로고
    • Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins
    • DOI 10.1016/S0924-2244(02)00133-4, PII S0924224402001334
    • M.A. de la Fuente, H. Singh, and Y. Hemar Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins Trends Food Sci. Tech. 13 2002 262 274 (Pubitemid 35436607)
    • (2002) Trends in Food Science and Technology , vol.13 , Issue.8 , pp. 262-274
    • De La Fuente, M.A.1    Singh, H.2    Hemar, Y.3
  • 8
    • 0037073089 scopus 로고    scopus 로고
    • Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of β-lactoglobulin AB
    • DOI 10.1016/S0021-9673(02)00884-1, PII S0021967302008841
    • Y. Surroca, J. Haverkamp, and A.J.R. Heck Towards the understanding of molecular mechanisms in the early stages of heat-induced aggregation of β-lactoglobulin AB J. Chromatogr. A 970 2002 275 285 (Pubitemid 35286583)
    • (2002) Journal of Chromatography A , vol.970 , Issue.1-2 , pp. 275-285
    • Surroca, Y.1    Haverkamp, J.2    Heck, A.J.R.3
  • 9
    • 0000008542 scopus 로고    scopus 로고
    • Heat-Induced Aggregation of β-Lactoglobulin: Role of the Free Thiol Group and Disulfide Bonds
    • M.A.M. Hoffmann, and P. van Mil Heat-induced aggregation of [beta]-lactoglobulin: role of the free thiol group and disulfide bonds J. Agr. Food Chem. 45 1997 2942 2948 (Pubitemid 127481834)
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.8 , pp. 2942-2948
    • Hoffmann, M.A.M.1    Van Mil, P.J.J.M.2
  • 10
    • 32944461715 scopus 로고    scopus 로고
    • Characterization of β-lactoglobulin-sodium alginate interactions in aqueous solutions: A calorimetry, light scattering, electrophoretic mobility and solubility study
    • DOI 10.1016/j.foodhyd.2005.05.005, PII S0268005X05000937
    • T. Harnsilawat, R. Pongsawatmanit, and D.J. McClements Characterization of β-lactoglobulin-sodium alginate interactions in aqueous solutions: a calorimetry, light scattering, electrophoretic mobility and solubility study Food Hydrocolloid 20 2006 577 585 (Pubitemid 43261606)
    • (2006) Food Hydrocolloids , vol.20 , Issue.5 , pp. 577-585
    • Harnsilawat, T.1    Pongsawatmanit, R.2    McClements, D.J.3
  • 11
    • 70149121260 scopus 로고    scopus 로고
    • Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry
    • I.J. Haug, H.M. Skar, G.E. Vegarud, T. Langsrud, and K.I. Draget Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry Food Hydrocolloid 23 2009 2287 2293
    • (2009) Food Hydrocolloid , vol.23 , pp. 2287-2293
    • Haug, I.J.1    Skar, H.M.2    Vegarud, G.E.3    Langsrud, T.4    Draget, K.I.5
  • 13
    • 0030272655 scopus 로고    scopus 로고
    • The effect of temperature and ionic strength on the dimerisation of β-lactoglobulin
    • DOI 10.1016/0141-8130(96)01130-0
    • P. Aymard, D. Durand, and T. Nicolai The effect of temperature and ionic strength on the dimerisation of β-lactoglobulin Int. J. Biol. Macromol. 19 1996 213 221 (Pubitemid 26354240)
    • (1996) International Journal of Biological Macromolecules , vol.19 , Issue.3 , pp. 213-221
    • Aymard, P.1    Durand, D.2    Nicolai, T.3
  • 14
    • 0032004945 scopus 로고    scopus 로고
    • Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies
    • DOI 10.1016/S0141-8130(97)00086-X, PII S014181309700086X
    • L. Renard, Griffin, Griffin, D. Renard, J. Lefebvre, M.C.A. Griffin, and W.G. Griffin Effects of Ph and salt environment on the association of beta-lactoglobulin revealed by intrinsic fluorescence studies Int. J. Biol. Macromol. 22 1998 41 49 (Pubitemid 28073619)
    • (1998) International Journal of Biological Macromolecules , vol.22 , Issue.1 , pp. 41-49
    • Renard, D.1    Lefebvre, J.2    Griffin, M.C.A.3    Griffin, W.G.4
  • 15
    • 0028985708 scopus 로고
    • Thermal denaturation of β-lactoglobulin: Effect of protein concentration at pH 6.75 and 8.05
    • X.L. Qi, S. Brownlow, C. Holt, and P. Sellers Thermal denaturation of β-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05 BBA-Protein Struct. M. 1248 1995 43 49
    • (1995) BBA-Protein Struct. M. , vol.1248 , pp. 43-49
    • Qi, X.L.1    Brownlow, S.2    Holt, C.3    Sellers, P.4
  • 16
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • X.L. Qi, C. Holt, D. McNulty, D.T. Clarke, S. Brownlow, and G.R. Jones Effect of temperature on the secondary structure of beta-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis Biochem. J. 324 1997 341
    • (1997) Biochem. J. , vol.324 , pp. 341
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 17
    • 84974326036 scopus 로고
    • Heat-induced changes in sulphydryl and disulphide levels of b-lactoglobulin A and the formation of polymers
    • K. Watanabe, and H. Klostermeyer Heat-induced changes in sulphydryl and disulphide levels of b-lactoglobulin A and the formation of polymers J. Dairy Res. 43 (3) 1976 411 418
    • (1976) J. Dairy Res. , vol.433 , pp. 411-418
    • Watanabe, K.1    Klostermeyer, H.2
  • 18
    • 84971943452 scopus 로고
    • A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160 °c
    • J.N. De Wit, and G. Klarenbeek A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160 °C J. Dairy Res. 48 1981 293 302
    • (1981) J. Dairy Res. , vol.48 , pp. 293-302
    • De Wit, J.N.1    Klarenbeek, G.2
  • 20
    • 52649129277 scopus 로고    scopus 로고
    • Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate
    • J.M. Jung, G. Savin, M. Pouzot, C. Schmitt, and R. Mezzenga Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate Biomacromolecules 9 2008 2477 2486
    • (2008) Biomacromolecules , vol.9 , pp. 2477-2486
    • Jung, J.M.1    Savin, G.2    Pouzot, M.3    Schmitt, C.4    Mezzenga, R.5
  • 21
    • 0001029829 scopus 로고
    • Surface coverage of beta-lactoglobulin at the oil-water interface - Influence of protein heat-treatment and various emulsifiers
    • E. Dickinson, and S.T. Hong Surface coverage of beta-lactoglobulin at the oil-water interface - influence of protein heat-treatment and various emulsifiers J. Agr. Food Chem. 42 1994 1602 1606
    • (1994) J. Agr. Food Chem. , vol.42 , pp. 1602-1606
    • Dickinson, E.1    Hong, S.T.2
  • 23
    • 1342293174 scopus 로고    scopus 로고
    • Conformational Transitions in β-Lactoglobulin Induced by Cationic Amphiphiles: Equilibrium Studies
    • M.I. Viseu, T.I. Carvalho, and S.M. Costa Conformational transitions in beta-lactoglobulin induced by cationic amphiphiles: equilibrium studies Biophys. J. 86 2004 2392 2402 (Pubitemid 38524427)
    • (2004) Biophysical Journal , vol.86 , Issue.4 , pp. 2392-2402
    • Viseu, M.I.1    Carvalho, T.I.2    Costa, S.M.B.3
  • 24
    • 36549015809 scopus 로고    scopus 로고
    • Unfolding kinetics of β-lactoglobulin induced by surfactant and denaturant: A stopped-flow/fluorescence study
    • DOI 10.1529/biophysj.106.101667
    • M.I. Viseu, E.P. Melo, T.I. Carvalho, R.F. Correia, and S.M. Costa Unfolding kinetics of beta-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study Biophys. J. 93 2007 3601 3612 (Pubitemid 350190823)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3601-3612
    • Viseu, M.I.1    Melo, E.P.2    Carvalho, T.I.3    Correia, R.F.4    Costa, S.M.B.5
  • 25
    • 2142837130 scopus 로고    scopus 로고
    • Heat treatment of whey proteins in the presence of anionic surfactants
    • H.J. Giroux, and M. Britten Heat treatment of whey proteins in the presence of anionic surfactants Food Hydrocolloid 18 2004 685 692
    • (2004) Food Hydrocolloid , vol.18 , pp. 685-692
    • Giroux, H.J.1    Britten, M.2
  • 26
    • 0029972943 scopus 로고    scopus 로고
    • Formation and structural heat-stability of β-lactoglobulin/ surfactant complexes
    • DOI 10.1016/0927-7765(96)01266-0
    • S. Magdassi, Y. Vinetsky, and P. Relkin Formation and structural heat-stability of beta-lactoglobulin/surfactant complexes Colloid Surface B 6 1996 353 362 (Pubitemid 26189656)
    • (1996) Colloids and Surfaces B: Biointerfaces , vol.6 , Issue.6 , pp. 353-362
    • Magdassi, S.1    Vinetsky, Y.2    Relkin, P.3
  • 27
    • 0031999031 scopus 로고    scopus 로고
    • Binding of sodium dodecyl sulphate and dodecyl trimethyl ammonium chloride to β-lactoglobulin: A calorimetric study
    • DOI 10.1016/S0958-6946(98)00031-4, PII S0958694698000314
    • R. Waninge, M. Paulsson, T. Nylander, B. Ninham, and P. Sellers Binding of sodium dodecyl sulphate and dodecyl trimethyl ammonium chloride to β-lactoglobulin: a calorimetric study Int. Dairy J. 8 1998 141 148 (Pubitemid 28434034)
    • (1998) International Dairy Journal , vol.8 , Issue.2 , pp. 141-148
    • Waninge, R.1    Paulsson, M.2    Nylander, T.3    Ninham, B.4    Sellers, P.5
  • 29
    • 0343081369 scopus 로고    scopus 로고
    • Salt-induced association of β-lactoglobulin by light and X-ray scattering
    • DOI 10.1021/ma990709u
    • G. Baldini, S. Beretta, G. Chirico, H. Franz, E. Maccioni, P. Mariani, and F. Spinozzis Salt-Induced association of [beta]-lactoglobulin by light and X-ray scattering Macromolecules 32 1999 6128 6138 (Pubitemid 30512097)
    • (1999) Macromolecules , vol.32 , Issue.19 , pp. 6128-6138
    • Baldini, G.1    Beretta, S.2    Chirico, G.3    Franz, H.4    Maccioni, E.5    Mariani, P.6    Spinozzi, F.7
  • 30
    • 0035824880 scopus 로고    scopus 로고
    • Characterization of pH-induced transitions of β-lactoglobulin: Ultrasonic, densimetric, and spectroscopic studies
    • DOI 10.1006/jmbi.2001.5188
    • N. Taulier, and T.V. Chalikian Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies J. Mol. Biol. 314 2001 873 889 (Pubitemid 34087854)
    • (2001) Journal of Molecular Biology , vol.314 , Issue.4 , pp. 873-889
    • Taulier, N.1    Chalikian, T.V.2
  • 31
    • 56049121413 scopus 로고    scopus 로고
    • α-Lactalbumin is unfolded by all classes of detergents but with different mechanisms
    • D.E. Otzen, P. Sehgal, and P. Westh α-Lactalbumin is unfolded by all classes of detergents but with different mechanisms J. Colloid Interf. Sci. 329 2009 273 283
    • (2009) J. Colloid Interf. Sci. , vol.329 , pp. 273-283
    • Otzen, D.E.1    Sehgal, P.2    Westh, P.3
  • 33
    • 2142760512 scopus 로고
    • Environmental effects on vibronic band intensities in pyrene monomer fluorescence and their application in studies of micellar systems
    • K. Kalyanasundaram, and J.K. Thomas Environmental effects on vibronic band intensities in pyrene monomer fluorescence and their application in studies of micellar systems J. Am. Chem. Soc. 99 1977 2039 2044
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 2039-2044
    • Kalyanasundaram, K.1    Thomas, J.K.2
  • 35
    • 77954758860 scopus 로고    scopus 로고
    • SDS-induced fibrillation of α-synuclein: An alternative fibrillation pathway
    • L. Giehm, C.L.P. Oliveira, G. Christiansen, J.S. Pedersen, D.E. Otzen, SDS-induced fibrillation of α-synuclein: an alternative fibrillation pathway, J. Mol. Biol. 401 (1) (2010) 115-133.
    • (2010) J. Mol. Biol. , vol.401 , Issue.1 , pp. 115-133
    • Giehm, L.1    Oliveira, C.L.P.2    Christiansen, G.3    Pedersen, J.S.4    Otzen, D.E.5
  • 36
    • 25144460975 scopus 로고    scopus 로고
    • Analysis of protein-surfactant interactions - A titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant
    • DOI 10.1016/j.bbapap.2005.08.001, PII S1570963905002499
    • A.D. Nielsen, L. Arleth, and P. Westh Analysis of protein-surfactant interactions-a titration calorimetric and fluorescence spectroscopic investigation of interactions between Humicola insolens cutinase and an anionic surfactant BBA-Proteins Proteom. 1752 2005 124 132 (Pubitemid 41338060)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1752 , Issue.2 , pp. 124-132
    • Nielsen, A.D.1    Arleth, L.2    Westh, P.3
  • 38
    • 38749136629 scopus 로고    scopus 로고
    • Global study of myoglobin-surfactant interactions
    • K.K. Andersen, P. Westh, and D.E. Otzen Global study of myoglobin-surfactant interactions Langmuir 24 2008 399 407
    • (2008) Langmuir , vol.24 , pp. 399-407
    • Andersen, K.K.1    Westh, P.2    Otzen, D.E.3
  • 40
    • 0014342404 scopus 로고
    • Binding of sodium dodecyl sulphate to various proteins
    • R. Pitt-Rivers, and F. Impiombato Binding of sodium dodecyl sulphate to various proteins Biochem. J. 109 1968 825 830
    • (1968) Biochem. J. , vol.109 , pp. 825-830
    • Pitt-Rivers, R.1    Impiombato, F.2
  • 41
    • 43049085820 scopus 로고    scopus 로고
    • Binding of phospholipids to beta-Lactoglobulin and their transfer to lipid bilayers
    • P.A. Martins, F. Gomes, W.L. Vaz, and M.J. Moreno Binding of phospholipids to beta-Lactoglobulin and their transfer to lipid bilayers Biochim. Biophys. Acta 1778 2008 1308 1315
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1308-1315
    • Martins, P.A.1    Gomes, F.2    Vaz, W.L.3    Moreno, M.J.4
  • 42
    • 0034633725 scopus 로고    scopus 로고
    • Interaction of beta-lactoglobulin with phospholipid bilayers: A molecular level elucidation as revealed by infrared spectroscopy
    • T. Lefevre, and M. Subirade Interaction of beta-lactoglobulin with phospholipid bilayers: a molecular level elucidation as revealed by infrared spectroscopy Int. J. Biol. Macromol. 28 2000 59 67
    • (2000) Int. J. Biol. Macromol. , vol.28 , pp. 59-67
    • Lefevre, T.1    Subirade, M.2
  • 43
    • 0034684161 scopus 로고    scopus 로고
    • The core lipocalin, bovine beta-lactoglobulin
    • L. Sawyer, and G. Kontopidis The core lipocalin, bovine beta-lactoglobulin Biochim. Biophys. Acta 1482 2000 136 148
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 136-148
    • Sawyer, L.1    Kontopidis, G.2
  • 45
    • 36549015809 scopus 로고    scopus 로고
    • Unfolding kinetics of β-lactoglobulin induced by surfactant and denaturant: A stopped-flow/fluorescence study
    • DOI 10.1529/biophysj.106.101667
    • M.I. Viseu, E.P. Melo, T.I. Carvalho, R.F. Correia, and S.M.B. Costa Unfolding kinetics of β-lactoglobulin induced by surfactant and denaturant: a stopped-flow/fluorescence study Biophys. J. 93 2007 3601 3612 (Pubitemid 350190823)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3601-3612
    • Viseu, M.I.1    Melo, E.P.2    Carvalho, T.I.3    Correia, R.F.4    Costa, S.M.B.5
  • 46
    • 79955602793 scopus 로고    scopus 로고
    • Structure-function relationship of β-lactoglobulin in the presence of dodecyltrimethyl ammonium bromide
    • A. Taheri-Kafrani, E. Asgari-Mobarakeh, A.K. Bordbar, and T. Haertlé Structure-function relationship of β-lactoglobulin in the presence of dodecyltrimethyl ammonium bromide Colloid Surface B 2009 2009
    • (2009) Colloid Surface B , pp. 2009
    • Taheri-Kafrani, A.1    Asgari-Mobarakeh, E.2    Bordbar, A.K.3    Haertlé, T.4
  • 47
    • 0001684352 scopus 로고
    • Surfactant interactions with biomembranes and proteins
    • M.N. Jones Surfactant interactions with biomembranes and proteins Chem. Soc. Rev. 21 1992 127 136
    • (1992) Chem. Soc. Rev. , vol.21 , pp. 127-136
    • Jones, M.N.1
  • 48
    • 0032843334 scopus 로고    scopus 로고
    • Heat-induced aggregation of beta-lactoglobulin as a function of pH
    • M.A. Hoffmann, and P.J. van Mil Heat-induced aggregation of beta-lactoglobulin as a function of pH J. Agr. Food Chem. 47 1999 1898 1905
    • (1999) J. Agr. Food Chem. , vol.47 , pp. 1898-1905
    • Hoffmann, M.A.1    Van Mil, P.J.2
  • 50
    • 0036787578 scopus 로고    scopus 로고
    • Protein unfolding in detergents: Effect of micelle structure, ionic strength, pH, and temperature
    • D.E. Otzen Protein unfolding in detergents: effect of micelle structure, ionic strength, pH, and temperature Biophys. J. 83 2002 2219 2230
    • (2002) Biophys. J. , vol.83 , pp. 2219-2230
    • Otzen, D.E.1
  • 51
    • 0033898830 scopus 로고    scopus 로고
    • Characterization and isolation of intermediates in β-lactoglobulin heat aggregation at high pH
    • R. Bauer, R. Carrotta, C. Rischel, and L. ∅gendal Characterization and isolation of intermediates in β-lactoglobulin heat aggregation at high pH Biophys. J. 79 2000 1030 1038 (Pubitemid 30626194)
    • (2000) Biophysical Journal , vol.79 , Issue.2 , pp. 1030-1038
    • Bauer, R.1    Carrotta, R.2    Rischel, C.3    Ogendal, L.4
  • 52
    • 0033501546 scopus 로고    scopus 로고
    • Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH
    • DOI 10.1016/S0958-6946(99)00148-X, PII S095869469900148X
    • E.P. Schokker, H. Singh, D.N. Pinder, G.E. Norris, and L.K. Creamer Characterization of intermediates formed during heat-induced aggregation of β-lactoglobulin AB at neutral pH Int. Dairy J. 9 1999 791 800 (Pubitemid 30147211)
    • (1999) International Dairy Journal , vol.9 , Issue.11 , pp. 791-800
    • Schokker, E.P.1    Singh, H.2    Pinder, D.N.3    Norris, G.E.4    Creamer, L.K.5
  • 53
    • 0032001691 scopus 로고    scopus 로고
    • Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin
    • DOI 10.1016/S0958-6946(98)00027-2, PII S0958694698000272
    • R. Bauer, S. Hansen, and L. ∅gendal Detection of intermediate oligomers, important for the formation of heat aggregates of β-lactoglobulin Int. Dairy J. 8 1998 105 112 (Pubitemid 28434029)
    • (1998) International Dairy Journal , vol.8 , Issue.2 , pp. 105-112
    • Bauer, R.1    Hansen, S.2    Ogendal, L.3
  • 54
    • 70350109497 scopus 로고    scopus 로고
    • How chain length and charge affect surfactant denaturation of acyl coenzyme A binding protein (ACBP)
    • K.K. Andersen, D.E. Otzen, How chain length and charge affect surfactant denaturation of acyl coenzyme A binding protein (ACBP), J. Phys. Chem. B 113 (2009), 13942-13952.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 13942-13952
    • Andersen, K.K.1    Otzen, D.E.2


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